Q5VZK9 (LR16A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leucine-rich repeat-containing protein 16A

Alternative name(s):
CARMIL homolog

Gene names

Name:	LRRC16A
Synonyms:	CARMIL, LRRC16

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1371 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds CAPZA2 with high affinity and significantly decreases CAPZA2 affinity for actin barbed ends. Increases the rate of elongation from seeds in the presence of CAPZA2, however, seems unable to nucleate filaments. Rapidly uncaps barbed ends capped by CAPZA2 and enhances barbed-end actin polymerization By similarity. Ref.3
Subunit structure	Interacts via its C-terminus with CAPZA2 in cytoplasm; interaction is essential for lamellipodial protrusion and cell translocation By similarity.
Subcellular location	Cytoplasm. Note: Colocalized with F-actin in lamellipodia but not with F-actin in stress fibers.
Tissue specificity	Expressed in lung, placenta, small intestine, liver, thymus, colon, skeletal muscle, heart and brain. Higher expression in kidney. Ref.3
Sequence similarities	Belongs to the CARMIL family. Contains 11 LRR (leucine-rich) repeats.
Sequence caution	The sequence BAA90912.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Leucine-rich repeat Repeat
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Non-traceable author statement PubMed 19846667. Source: BHF-UCL blood coagulation Traceable author statement. Source: Reactome cell migration Inferred from mutant phenotype PubMed 19846667. Source: BHF-UCL lamellipodium assembly Inferred from mutant phenotype PubMed 19846667. Source: BHF-UCL ruffle organization Inferred from mutant phenotype PubMed 19846667. Source: BHF-UCL urate metabolic process Inferred from mutant phenotype PubMed 19503597. Source: BHF-UCL
Cellular_component	cytosol Traceable author statement. Source: Reactome lamellipodium Inferred from direct assay PubMed 19846667. Source: BHF-UCL nucleus Inferred from direct assay. Source: HPA
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5VZK9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Gene prediction based on EST data.

Isoform 2 (identifier: Q5VZK9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1177-1221: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q5VZK9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     486-499: SLDISDNGLESDLS → QLGTRYRNAVLRVY
     500-1371: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q5VZK9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.
     292-337: GVSSLSIQFA...SLSANPLTAS → ETTTKIKRQN...NYYSDFSHDG
     338-1371: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1371

1371

Leucine-rich repeat-containing protein 16A

PRO_0000325815

Regions

Repeat

245 – 269

25

LRR 1

Repeat

275 – 298

24

LRR 2

Repeat

304 – 327

24

LRR 3

Repeat

336 – 363

28

LRR 4

Repeat

391 – 418

28

LRR 5

Repeat

423 – 447

25

LRR 6

Repeat

481 – 506

26

LRR 7

Repeat

543 – 566

24

LRR 8

Repeat

570 – 593

24

LRR 9

Repeat

654 – 678

25

LRR 10

Repeat

958 – 981

24

LRR 11

Region

958 – 1082

125

Inhibits capping activity of CAPZA2 By similarity

Coiled coil

710 – 734

25

Potential

Compositional bias

1243 – 1250

8

Poly-Ser

Amino acid modifications

Modified residue

916

1

Phosphothreonine Ref.5

Modified residue

968

1

Phosphoserine Ref.5 Ref.6 Ref.9

Modified residue

1067

1

Phosphoserine Ref.7

Modified residue

1288

1

Phosphoserine Ref.5 Ref.7 Ref.9

Modified residue

1291

1

Phosphoserine Ref.5

Modified residue

1315

1

Phosphoserine Ref.9

Modified residue

1331

1

Phosphoserine Ref.5 Ref.7 Ref.9

Modified residue

1360

1

Phosphoserine Ref.9

Cross-link

593

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4

Natural variations

Alternative sequence

1 – 161

161

Missing in isoform 4.

VSP_032415

Alternative sequence

292 – 337

46

GVSSL…PLTAS → ETTTKIKRQNVPTVLQTYLV VCPSDYQPCPLPLGKDNYYS DFSHDG in isoform 4.

VSP_032416

Alternative sequence

338 – 1371

1034

Missing in isoform 4.

VSP_032417

Alternative sequence

486 – 499

14

SLDIS…ESDLS → QLGTRYRNAVLRVY in isoform 3.

VSP_032418

Alternative sequence

500 – 1371

872

Missing in isoform 3.

VSP_032419

Alternative sequence

1177 – 1221

45

Missing in isoform 2.

VSP_032420

Natural variant

77

1

V → I.
Corresponds to variant rs9358856 [ dbSNP | Ensembl ].

VAR_039923

Natural variant

545

1

P → L.
Corresponds to variant rs12207840 [ dbSNP | Ensembl ].

VAR_039924

Natural variant

639

1

A → G.
Corresponds to variant rs7454756 [ dbSNP | Ensembl ].

VAR_039925

Natural variant

1117

1

N → S.
Corresponds to variant rs9885914 [ dbSNP | Ensembl ].

VAR_039926

Experimental info

Sequence conflict

255

1

N → D in BAC85701. Ref.1

Sequence conflict

889

1

K → R in BAA90912. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

1371

Helix Strand Turn

Details...

Beta strand

978 – 980

3

Helix

985 – 988

4

Beta strand

999 – 1002

4

Helix

1026 – 1029

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 6DECD6387FD73DCE	FASTA	1,371	151,557
	10 20 30 40 50 60 MTEESSDVPR ELIESIKDVI GRKIKISVKK KVKLEVKGDK VENKVLVLTS CRAFLVTARI 70 80 90 100 110 120 PTKLELTFSY LEIHGVVCSK SAQMIVETEK CSISMKMASP EDVSEVLAHI GTCLRKIFPG 130 140 150 160 170 180 LSPVRIMKKV SMEPSERLAS LQALWDSQTV AEQGPCGGFS QMYACVCDWL GFSYREEVQW 190 200 210 220 230 240 DVDTIYLTQD TRELNLQDFS HLDHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR 250 260 270 280 290 300 VVSRSNRLEE LVLENAGLRT DFAQKLASAL AHNPNSGLHT INLAGNPLED RGVSSLSIQF 310 320 330 340 350 360 AKLPKGLKHL NLSKTSLSPK GVNSLSQSLS ANPLTASTLV HLDLSGNVLR GDDLSHMYNF 370 380 390 400 410 420 LAQPNAIVHL DLSNTECSLD MVCGALLRGC LQYLAVLNLS RTVFSHRKGK EVPPSFKQFF 430 440 450 460 470 480 SSSLALMHIN LSGTKLSPEP LKALLLGLAC NHNLKGVSLD LSNCELRSGG AQVLEGCIAE 490 500 510 520 530 540 IHNITSLDIS DNGLESDLST LIVWLSKNRS IQHLALGKNF NNMKSKNLTP VLDNLVQMIQ 550 560 570 580 590 600 DEESPLQSLS LADSKLKTEV TIIINALGSN TSLTKVDISG NGMGDMGAKM LAKALQINTK 610 620 630 640 650 660 LRTVIWDKNN ITAQGFQDIA VAMEKNYTLR FMPIPMYDAS QALKTNPEKT EDALQKIENY 670 680 690 700 710 720 LLRNHETRKY LQEQAYRLQQ GIVTSTTQQM IDRICVKVQD HLNSLRNCGG DAIQEDLKSA 730 740 750 760 770 780 ERLMRDAKNS KTLLPNLYHV GGASWAGASG LLSSPIQETL ESMAGEVTRV VDEQLKALLE 790 800 810 820 830 840 SMVDAAENLC PNVMKKAHIR QDLIHASTEK ISIPRTFVKN VLLEQSGIDI LNKISEVKLT 850 860 870 880 890 900 VASFLSDRIV DEILDALSHC HHKLADHFSR RGKTLPQQES LEIELAEEKP VKRSIITVEE 910 920 930 940 950 960 LTEIERLEDL DTCMMTPKSK RKSIHSRMLR PVSRAFEMEF DLDKALEEVP IHIEDPPFPS 970 980 990 1000 1010 1020 LRQEKRSSGF ISELPSEEGK KLEHFTKLRP KRNKKQQPTQ AAVCAANIVS QDGEQNGLMG 1030 1040 1050 1060 1070 1080 RVDEGVDEFF TKKVTKMDSK KWSTRGSESH ELNEGGDEKK KRDSRKSSGF LNLIKSRSKS 1090 1100 1110 1120 1130 1140 ERPPTILMTE EPSSPKGAVR SPPVDCPRKD TKAAEHNGNS ERIEEIKTPD SFEESQGEEI 1150 1160 1170 1180 1190 1200 GKVERSDSKS SPQAGRRYGV QVMGSGLLAE MKAKQEKRAA CAQKKLGNDA VSQDSSSPAL 1210 1220 1230 1240 1250 1260 SGVERSDGGG AVPKLHPGLP ENRFGLGTPE KNTKAEPKAE AGSRSRSSSS TPTSPKPLLQ 1270 1280 1290 1300 1310 1320 SPKPSLAARP VIPQKPRTAS RPDDIPDSPS SPKVALLPPV LKKVPSDKER DGQSSPQPSP 1330 1340 1350 1360 1370 RTFSQEVSRR SWGQQAQEYQ EQKQRSSSKD GHQGSKSNDS GEEAEKEFIF V
	Isoform 2 [UniParc]. Checksum: BC4881025483CA27	FASTA	1,326	147,088
	10 20 30 40 50 60 MTEESSDVPR ELIESIKDVI GRKIKISVKK KVKLEVKGDK VENKVLVLTS CRAFLVTARI 70 80 90 100 110 120 PTKLELTFSY LEIHGVVCSK SAQMIVETEK CSISMKMASP EDVSEVLAHI GTCLRKIFPG 130 140 150 160 170 180 LSPVRIMKKV SMEPSERLAS LQALWDSQTV AEQGPCGGFS QMYACVCDWL GFSYREEVQW 190 200 210 220 230 240 DVDTIYLTQD TRELNLQDFS HLDHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR 250 260 270 280 290 300 VVSRSNRLEE LVLENAGLRT DFAQKLASAL AHNPNSGLHT INLAGNPLED RGVSSLSIQF 310 320 330 340 350 360 AKLPKGLKHL NLSKTSLSPK GVNSLSQSLS ANPLTASTLV HLDLSGNVLR GDDLSHMYNF 370 380 390 400 410 420 LAQPNAIVHL DLSNTECSLD MVCGALLRGC LQYLAVLNLS RTVFSHRKGK EVPPSFKQFF 430 440 450 460 470 480 SSSLALMHIN LSGTKLSPEP LKALLLGLAC NHNLKGVSLD LSNCELRSGG AQVLEGCIAE 490 500 510 520 530 540 IHNITSLDIS DNGLESDLST LIVWLSKNRS IQHLALGKNF NNMKSKNLTP VLDNLVQMIQ 550 560 570 580 590 600 DEESPLQSLS LADSKLKTEV TIIINALGSN TSLTKVDISG NGMGDMGAKM LAKALQINTK 610 620 630 640 650 660 LRTVIWDKNN ITAQGFQDIA VAMEKNYTLR FMPIPMYDAS QALKTNPEKT EDALQKIENY 670 680 690 700 710 720 LLRNHETRKY LQEQAYRLQQ GIVTSTTQQM IDRICVKVQD HLNSLRNCGG DAIQEDLKSA 730 740 750 760 770 780 ERLMRDAKNS KTLLPNLYHV GGASWAGASG LLSSPIQETL ESMAGEVTRV VDEQLKALLE 790 800 810 820 830 840 SMVDAAENLC PNVMKKAHIR QDLIHASTEK ISIPRTFVKN VLLEQSGIDI LNKISEVKLT 850 860 870 880 890 900 VASFLSDRIV DEILDALSHC HHKLADHFSR RGKTLPQQES LEIELAEEKP VKRSIITVEE 910 920 930 940 950 960 LTEIERLEDL DTCMMTPKSK RKSIHSRMLR PVSRAFEMEF DLDKALEEVP IHIEDPPFPS 970 980 990 1000 1010 1020 LRQEKRSSGF ISELPSEEGK KLEHFTKLRP KRNKKQQPTQ AAVCAANIVS QDGEQNGLMG 1030 1040 1050 1060 1070 1080 RVDEGVDEFF TKKVTKMDSK KWSTRGSESH ELNEGGDEKK KRDSRKSSGF LNLIKSRSKS 1090 1100 1110 1120 1130 1140 ERPPTILMTE EPSSPKGAVR SPPVDCPRKD TKAAEHNGNS ERIEEIKTPD SFEESQGEEI 1150 1160 1170 1180 1190 1200 GKVERSDSKS SPQAGRRYGV QVMGSGLLAE MKAKQENRFG LGTPEKNTKA EPKAEAGSRS 1210 1220 1230 1240 1250 1260 RSSSSTPTSP KPLLQSPKPS LAARPVIPQK PRTASRPDDI PDSPSSPKVA LLPPVLKKVP 1270 1280 1290 1300 1310 1320 SDKERDGQSS PQPSPRTFSQ EVSRRSWGQQ AQEYQEQKQR SSSKDGHQGS KSNDSGEEAE KEFIFV
	Isoform 3 [UniParc]. Checksum: A77D54FABEE374C8	FASTA	499	55,117
	10 20 30 40 50 60 MTEESSDVPR ELIESIKDVI GRKIKISVKK KVKLEVKGDK VENKVLVLTS CRAFLVTARI 70 80 90 100 110 120 PTKLELTFSY LEIHGVVCSK SAQMIVETEK CSISMKMASP EDVSEVLAHI GTCLRKIFPG 130 140 150 160 170 180 LSPVRIMKKV SMEPSERLAS LQALWDSQTV AEQGPCGGFS QMYACVCDWL GFSYREEVQW 190 200 210 220 230 240 DVDTIYLTQD TRELNLQDFS HLDHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR 250 260 270 280 290 300 VVSRSNRLEE LVLENAGLRT DFAQKLASAL AHNPNSGLHT INLAGNPLED RGVSSLSIQF 310 320 330 340 350 360 AKLPKGLKHL NLSKTSLSPK GVNSLSQSLS ANPLTASTLV HLDLSGNVLR GDDLSHMYNF 370 380 390 400 410 420 LAQPNAIVHL DLSNTECSLD MVCGALLRGC LQYLAVLNLS RTVFSHRKGK EVPPSFKQFF 430 440 450 460 470 480 SSSLALMHIN LSGTKLSPEP LKALLLGLAC NHNLKGVSLD LSNCELRSGG AQVLEGCIAE 490 IHNITQLGTR YRNAVLRVY
	Isoform 4 [UniParc]. Checksum: 806D8D31AAC2A04A	FASTA	176	20,181
	10 20 30 40 50 60 MYACVCDWLG FSYREEVQWD VDTIYLTQDT RELNLQDFSH LDHRDLIPII AALEYNQWFT 70 80 90 100 110 120 KLSSKDLKLS TDVCEQILRV VSRSNRLEEL VLENAGLRTD FAQKLASALA HNPNSGLHTI 130 140 150 160 170 NLAGNPLEDR ETTTKIKRQN VPTVLQTYLV VCPSDYQPCP LPLGKDNYYS DFSHDG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 766-1371 (ISOFORM 2). Tissue: Colon, Esophageal carcinoma and Teratocarcinoma.
[2]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Mammalian CARMIL inhibits actin filament capping by capping protein." Yang C., Pring M., Wear M.A., Huang M., Cooper J.A., Svitkina T.M., Zigmond S.H. Dev. Cell 9:209-221(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[4]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-593, MASS SPECTROMETRY. Tissue: Mammary cancer.
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-916; SER-968; SER-1288; SER-1291 AND SER-1331, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067; SER-1288 AND SER-1331, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968; SER-1288; SER-1315; SER-1331 AND SER-1360, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK123817 mRNA. Translation: BAC85701.1.
AK125696 mRNA. Translation: BAC86250.1.
AK000055 mRNA. Translation: BAA90912.1. Different initiation.
AL160037, AL022170, AL024509 Genomic DNA. Translation: CAH72024.1.
AL022170, AL024509, AL160037 Genomic DNA. Translation: CAI21583.1.
AL024509, AL022170, AL160037 Genomic DNA. Translation: CAI21665.1.

IPI

IPI00014843.
IPI00446337.
IPI00873593.
IPI00887902.

RefSeq

NP_060110.4. NM_017640.5.

UniGene

Hs.649550.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LK2	X-ray	2.20	T	961-1012	[»]
3LK3	X-ray	2.68	T	964-1078	[»]

ProteinModelPortal

Q5VZK9.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-56920N.

IntAct

Q5VZK9. 1 interaction.

STRING

9606.ENSP00000331983.

PTM databases

PhosphoSite

Q5VZK9.

Polymorphism databases

DMDM

74762279.

Proteomic databases

PaxDb

Q5VZK9.

PeptideAtlas

Q5VZK9.

PRIDE

Q5VZK9.

Protocols and materials databases

DNASU

55604.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000329474; ENSP00000331983; ENSG00000079691.
ENST00000377969; ENSP00000367206; ENSG00000079691.

GeneID

55604.

KEGG

hsa:55604.

UCSC

uc003nez.1. human.
uc011djw.2. human.

Organism-specific databases

CTD

55604.

GeneCards

GC06P025279.

H-InvDB

HIX0005632.

HGNC

HGNC:21581. LRRC16A.

HPA

HPA029038.
HPA029039.

MIM

609593. gene.

neXtProt

NX_Q5VZK9.

PharmGKB

PA162394368.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG239526.

HOGENOM

HOG000230565.

HOVERGEN

HBG108094.

InParanoid

Q5VZK9.

OMA

TLIVWLS.

OrthoDB

EOG4GTKC4.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

Bgee

Q5VZK9.

CleanEx

HS_LRRC16A.

Genevestigator

Q5VZK9.

Family and domain databases

ProtoNet

Search...

Other

ChiTaRS

LRRC16A. human.

EvolutionaryTrace

Q5VZK9.

GenomeRNAi

55604.

NextBio

60153.

SOURCE

Search...

Entry information

Entry name

LR16A_HUMAN

Accession

Primary (citable) accession number: Q5VZK9
Secondary accession number(s): Q6ZUH5, Q6ZW07, Q9NXU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	December 7, 2004
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.